ID   EMIL2_HUMAN             Reviewed;        1053 AA.
AC   Q9BXX0; B2RMY3; Q8NBH3; Q96JQ4;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   25-MAY-2022, entry version 156.
DE   RecName: Full=EMILIN-2;
DE   AltName: Full=Elastin microfibril interface-located protein 2;
DE            Short=Elastin microfibril interfacer 2;
DE   AltName: Full=Protein FOAP-10;
DE   Flags: Precursor;
GN   Name=EMILIN2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-903.
RC   TISSUE=Kidney;
RX   PubMed=11278945; DOI=10.1074/jbc.m011591200;
RA   Doliana R., Bot S., Mungiguerra G., Canton A., Cilli S.P., Colombatti A.;
RT   "Isolation and characterization of EMILIN-2, a new component of the growing
RT   EMILINs family and a member of the EMI domain-containing superfamily.";
RL   J. Biol. Chem. 276:12003-12011(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16177791; DOI=10.1038/nature03983;
RA   Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA   Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA   Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA   Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA   Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA   Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA   Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA   Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 18.";
RL   Nature 437:551-555(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 590-1053.
RC   TISSUE=Adrenal gland;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 846-1053.
RC   TISSUE=Macrophage;
RA   Fujii Y., Takayama K., Tsuritani K., Yajima Y., Amemiya T., Ukai Y.,
RA   Naito K., Kawaguchi A.;
RT   "Homo sapiens mRNA for FOAP-10 protein, partial cds.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-616.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
CC   -!- FUNCTION: May be responsible for anchoring smooth muscle cells to
CC       elastic fibers, and may be involved not only in the formation of the
CC       elastic fiber, but also in the processes that regulate vessel assembly.
CC       Has cell adhesive capacity.
CC   -!- SUBUNIT: Homotrimer associated through a moderately stable interaction
CC       of the C-terminal globular C1q domains, allowing the nucleation of the
CC       triple helix and then a further quaternary assembly to higher-order
CC       polymers via intermolecular disulfide bonds (By similarity). Interacts
CC       with EMILIN1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix. Note=Found mainly at the interface between amorphous elastin
CC       and microfibrils.
CC   -!- TISSUE SPECIFICITY: Highest levels are present in fetal heart and adult
CC       lung. Intermediate levels in peripheral leukocytes, placenta, and
CC       spinal cord and low expression in fetal brain, spleen, thymus, and lung
CC       and in adult heart, aorta, testis, bone marrow, small intestine,
CC       thymus, lymph node, and appendix.
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DR   EMBL; AF270513; AAK37963.1; -; mRNA.
DR   EMBL; AP000919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471113; EAX01690.1; -; Genomic_DNA.
DR   EMBL; BC136541; AAI36542.1; -; mRNA.
DR   EMBL; AK090519; BAC03470.1; -; mRNA.
DR   EMBL; AB026706; BAB61020.1; -; mRNA.
DR   CCDS; CCDS11828.1; -.
DR   RefSeq; NP_114437.2; NM_032048.2.
DR   AlphaFoldDB; Q9BXX0; -.
DR   SMR; Q9BXX0; -.
DR   BioGRID; 123848; 26.
DR   ComplexPortal; CPX-436; EMILIN-2 complex.
DR   IntAct; Q9BXX0; 11.
DR   STRING; 9606.ENSP00000254528; -.
DR   GlyGen; Q9BXX0; 23 sites, 3 O-linked glycans (13 sites).
DR   iPTMnet; Q9BXX0; -.
DR   PhosphoSitePlus; Q9BXX0; -.
DR   BioMuta; EMILIN2; -.
DR   DMDM; 296439365; -.
DR   EPD; Q9BXX0; -.
DR   jPOST; Q9BXX0; -.
DR   MassIVE; Q9BXX0; -.
DR   MaxQB; Q9BXX0; -.
DR   PaxDb; Q9BXX0; -.
DR   PeptideAtlas; Q9BXX0; -.
DR   PRIDE; Q9BXX0; -.
DR   ProteomicsDB; 79535; -.
DR   Antibodypedia; 21912; 57 antibodies from 17 providers.
DR   DNASU; 84034; -.
DR   Ensembl; ENST00000254528.4; ENSP00000254528.3; ENSG00000132205.11.
DR   GeneID; 84034; -.
DR   KEGG; hsa:84034; -.
DR   MANE-Select; ENST00000254528.4; ENSP00000254528.3; NM_032048.3; NP_114437.2.
DR   UCSC; uc002kln.4; human.
DR   CTD; 84034; -.
DR   DisGeNET; 84034; -.
DR   GeneCards; EMILIN2; -.
DR   HGNC; HGNC:19881; EMILIN2.
DR   HPA; ENSG00000132205; Tissue enhanced (parathyroid).
DR   MIM; 608928; gene.
DR   neXtProt; NX_Q9BXX0; -.
DR   OpenTargets; ENSG00000132205; -.
DR   PharmGKB; PA134880588; -.
DR   VEuPathDB; HostDB:ENSG00000132205; -.
DR   eggNOG; ENOG502QV5P; Eukaryota.
DR   GeneTree; ENSGT01030000234633; -.
DR   HOGENOM; CLU_011705_0_0_1; -.
DR   InParanoid; Q9BXX0; -.
DR   OMA; NIQGKPH; -.
DR   OrthoDB; 1205089at2759; -.
DR   PhylomeDB; Q9BXX0; -.
DR   TreeFam; TF331033; -.
DR   PathwayCommons; Q9BXX0; -.
DR   Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR   SignaLink; Q9BXX0; -.
DR   BioGRID-ORCS; 84034; 8 hits in 1066 CRISPR screens.
DR   ChiTaRS; EMILIN2; human.
DR   GenomeRNAi; 84034; -.
DR   Pharos; Q9BXX0; Tbio.
DR   PRO; PR:Q9BXX0; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; Q9BXX0; protein.
DR   Bgee; ENSG00000132205; Expressed in decidua and 167 other tissues.
DR   Genevisible; Q9BXX0; HS.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0030023; F:extracellular matrix constituent conferring elasticity; NAS:UniProtKB.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IC:ComplexPortal.
DR   GO; GO:0030336; P:negative regulation of cell migration; IDA:ComplexPortal.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IDA:ComplexPortal.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IDA:ComplexPortal.
DR   GO; GO:0030194; P:positive regulation of blood coagulation; IEA:Ensembl.
DR   GO; GO:1900426; P:positive regulation of defense response to bacterium; IDA:ComplexPortal.
DR   GO; GO:1901731; P:positive regulation of platelet aggregation; IDA:ComplexPortal.
DR   GO; GO:0008217; P:regulation of blood pressure; IC:ComplexPortal.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IC:ComplexPortal.
DR   Gene3D; 2.60.120.40; -; 1.
DR   InterPro; IPR001073; C1q_dom.
DR   InterPro; IPR011489; EMI_domain.
DR   InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR   Pfam; PF00386; C1q; 1.
DR   Pfam; PF07546; EMI; 1.
DR   SMART; SM00110; C1Q; 1.
DR   SUPFAM; SSF49842; SSF49842; 1.
DR   PROSITE; PS50871; C1Q; 1.
DR   PROSITE; PS51041; EMI; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion; Coiled coil; Collagen; Disulfide bond; Extracellular matrix;
KW   Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..1053
FT                   /note="EMILIN-2"
FT                   /id="PRO_0000007817"
FT   DOMAIN          44..120
FT                   /note="EMI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT   DOMAIN          840..892
FT                   /note="Collagen-like"
FT   DOMAIN          901..1052
FT                   /note="C1q"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT   REGION          120..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          783..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          177..215
FT                   /evidence="ECO:0000255"
FT   COILED          253..340
FT                   /evidence="ECO:0000255"
FT   COILED          369..389
FT                   /evidence="ECO:0000255"
FT   COILED          578..634
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        143..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        786..815
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        458
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        510
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        587
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        616
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   CARBOHYD        745
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        974
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        48..110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT   DISULFID        74..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT   DISULFID        109..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT   VARIANT         215
FT                   /note="A -> T (in dbSNP:rs16943977)"
FT                   /id="VAR_057528"
FT   VARIANT         259
FT                   /note="M -> V (in dbSNP:rs35267664)"
FT                   /id="VAR_057529"
FT   VARIANT         903
FT                   /note="P -> S (in dbSNP:rs56288451)"
FT                   /evidence="ECO:0000269|PubMed:11278945"
FT                   /id="VAR_062003"
FT   CONFLICT        545
FT                   /note="K -> G (in Ref. 1; AAK37963)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1053 AA;  115687 MW;  9F2895AB0AC5E8EF CRC64;
     MWQPRRPWPR VPWRWALALL ALVGAGLCHA GPQPGYPARP SARNKNWCAY IVNKNVSCSV
     LEGSESFIQA QYNCAWNQMP CPSALVYRVN FRPRYVTRYK TVTQLEWRCC PGFRGGDCQE
     GPKDPVKTLR PTPARPRNSL KKATDNEPSQ FSEPRKTLSP TGTAQPSWGV DPKEGPQELQ
     EKKIQVLEEK VLRLTRTVLD LQSSLAGVSE NLKHATQDDA SRTRAPGLSS QHPKPDTTVS
     GDTETGQSPG VFNTKESGMK DIKSELAEVK DTLKNKSDKL EELDGKVKGY EGQLRQLQEA
     AQGPTVTMTT NELYQAYVDS KIDALREELM EGMDRKLADL KNSCEYKLTG LQQQCDDYGS
     SYLGVIELIG EKETSLRKEI NNLRARLQEP SAQANCCDSE KNGDIGQQIK TLDQKIERVA
     EATRMLNGRL DNEFDRLIVP EPDVDFDAKW NELDARINVT EKNAEEHCFY IEETLRGAIN
     GEVGDLKQLV DQKIQSLEDR LGSVLLQMTN NTGAELSPPG AAALPGVSGS GDERVMMELN
     HLKDKVQVVE DICLLNIQGK PHGMEGALPN REDRAVRDSL HLLKSLNDTM HRKFQETEQT
     IQKLQQDFSF LYSQLNHTEN DVTHLQKEMS NCRAGENAGM GRFTKVGEQE RTVDTLPSPQ
     HPVAHCCSQL EERWQRLQSQ VISELDACKE CTQGVQREVS MVEGRVSHME KTCSKLDSIS
     GNLQRIKEGL NKHVSSLWNC VRQMNGTLRS HSRDISGLKN SVQQFYSHVF QISTDLQDLV
     KFQPSAKAPS PPPPAEAPKE PLQPEPAPPR PSGPATAEDP GRRPVLPQRP PEERPPQPPG
     STGVIAETGQ AGPPAGAGVS GRGLPRGVDG QTGSGTVPGA EGFAGAPGYP KSPPVASPGA
     PVPSLVSFSA GLTQKPFPSD GGVVLFNKVL VNDGDVYNPS TGVFTAPYDG RYLITATLTP
     ERDAYVEAVL SVSNASVAQL HTAGYRREFL EYHRPPGALH TCGGPGAFHL IVHLKAGDAV
     NVVVTGGKLA HTDFDEMYST FSGVFLYPFL SHL
//